Human eye lens proteins are known for their stability and longevity but due to their long lifespan are prone to a variety of post-translation modifications1. These modification tend to appear as a function of age and are especially common in the lenses of eyes afflicted with cataract. It is thought that the build up of modification in these proteins leads to loss of structural stability, resulting in aggregation and lens cloudiness1. Peptides that correspond to fragments of a known truncation modification in the eye lens proteins βA3- and γS-Crystallin are reported to take up an alpha helical structure in membrane mimicking conditions2. NMR studies where used to determine the extent of secondary structure exhibited by these peptides. Secondary chemical shifts and backbone NOE constraints derived from two dimensional 1H and 13C NMR show an α-heilical tendency in both peptides. Further structural calculation using NOE distance and dihedral bond angle restraints have produced structures for each peptide showing strong helical structure in the γS-Crystallin fragment and weaker helical tendency in the βA3-Crystallin peptide.